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Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2.

[beta]-Arrestins are multifunctional adaptors that mediate the desensitization, internalization, and some signaling functions of seven-transmembrane receptors (7TMRs). Agonist-stimulated ubiquitination of [beta]-arrestin2 mediated by the E3 ubiquitin ligase Mdm2 is critical for rapid [[beta].sub.2]-... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America April 21, 2009, Vol.106(16), pp.6650-6655
Main Author: Shenoy, Sudha K
Other Authors: Modi, Aalok S , Shukla, Arun K , Xiao, Kunhong , Berthouze, Magali , Ahn, Seungkirl , Wilkinson, Keith D , Miller, William E , Lefkowitz, Robert J
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.0901083106
Link: http://search.proquest.com/docview/67207909/?pq-origsite=primo
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title: Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2.
format: Article
creator:
  • Shenoy, Sudha K
  • Modi, Aalok S
  • Shukla, Arun K
  • Xiao, Kunhong
  • Berthouze, Magali
  • Ahn, Seungkirl
  • Wilkinson, Keith D
  • Miller, William E
  • Lefkowitz, Robert J
subjects:
  • Animals–Metabolism
  • Arrestins–Drug Effects
  • Cell Line–Enzymology
  • Endosomes–Drug Effects
  • Enzyme Activation–Metabolism
  • Extracellular Signal-Regulated MAP Kinases–Drug Effects
  • Humans–Drug Effects
  • Kinetics–Metabolism
  • Models, Biological–Metabolism
  • Protein Binding–Drug Effects
  • Protein Transport–Metabolism
  • Proto-Oncogene Proteins C-Mdm2–Metabolism
  • Receptors, Cell Surface–Drug Effects
  • Signal Transduction–Pharmacology
  • Ubiquitin Thiolesterase–Pharmacology
  • Ubiquitin-Protein Ligases–Pharmacology
  • Ubiquitination–Pharmacology
  • Vasopressins–Pharmacology
  • Beta-Arrestins–Pharmacology
  • Arrestins
  • Receptors, Cell Surface
  • Beta-Arrestins
  • Vasopressins
  • Mdm2 Protein, Human
  • Proto-Oncogene Proteins C-Mdm2
  • Ubiquitin-Protein Ligases
  • Extracellular Signal-Regulated MAP Kinases
  • Usp33 Protein, Human
  • Ubiquitin Thiolesterase
ispartof: Proceedings of the National Academy of Sciences of the United States of America, April 21, 2009, Vol.106(16), pp.6650-6655
description: [beta]-Arrestins are multifunctional adaptors that mediate the desensitization, internalization, and some signaling functions of seven-transmembrane receptors (7TMRs). Agonist-stimulated ubiquitination of [beta]-arrestin2 mediated by the E3 ubiquitin ligase Mdm2 is critical for rapid [[beta].sub.2]-adrenergic receptor ([[beta].sub.2]AR) internalization. We now report the discovery that the deubiquitinating enzyme ubiquitin-specific protease 33 (USP33) binds [beta]-arrestin2 and leads to the deubiquitination of [beta]-arrestins. USP33 and Mdm2 function reciprocally and favor respectively the stability or lability of the receptor [beta]-arrestin complex, thus regulating the longevity and subcellular localization of receptor signalosomes. Receptors such as the [[beta].sub.2]AR, previously shown to form loose complexes with [beta]-arrestin ("class A") promote a [beta]-arrestin conformation conducive for binding to the deubiquitinase, whereas the vasopressin V2R, which forms tight [beta]-arrestin complexes ("class B"), promotes a distinct [beta]-arrestin conformation that favors dissociation of the enzyme. Thus, USP33-[beta]-arrestin interaction is a key regulatory step in 7TMR trafficking and signal transmission from the activated receptors to downstream effectors. endocytosis | G protein-coupled receptors | ubiquitination | phosphorylation | ERK 1/2
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.0901083106
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleBeta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2.
creatorShenoy, Sudha K ; Modi, Aalok S ; Shukla, Arun K ; Xiao, Kunhong ; Berthouze, Magali ; Ahn, Seungkirl ; Wilkinson, Keith D ; Miller, William E ; Lefkowitz, Robert J
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identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.0901083106
subjectAnimals–Metabolism ; Arrestins–Drug Effects ; Cell Line–Enzymology ; Endosomes–Drug Effects ; Enzyme Activation–Metabolism ; Extracellular Signal-Regulated MAP Kinases–Drug Effects ; Humans–Drug Effects ; Kinetics–Metabolism ; Models, Biological–Metabolism ; Protein Binding–Drug Effects ; Protein Transport–Metabolism ; Proto-Oncogene Proteins C-Mdm2–Metabolism ; Receptors, Cell Surface–Drug Effects ; Signal Transduction–Pharmacology ; Ubiquitin Thiolesterase–Pharmacology ; Ubiquitin-Protein Ligases–Pharmacology ; Ubiquitination–Pharmacology ; Vasopressins–Pharmacology ; Beta-Arrestins–Pharmacology ; Arrestins ; Receptors, Cell Surface ; Beta-Arrestins ; Vasopressins ; Mdm2 Protein, Human ; Proto-Oncogene Proteins C-Mdm2 ; Ubiquitin-Protein Ligases ; Extracellular Signal-Regulated MAP Kinases ; Usp33 Protein, Human ; Ubiquitin Thiolesterase
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description[beta]-Arrestins are multifunctional adaptors that mediate the desensitization, internalization, and some signaling functions of seven-transmembrane receptors (7TMRs). Agonist-stimulated ubiquitination of [beta]-arrestin2 mediated by the E3 ubiquitin ligase Mdm2 is critical for rapid [[beta].sub.2]-adrenergic receptor ([[beta].sub.2]AR) internalization. We now report the discovery that the deubiquitinating enzyme ubiquitin-specific protease 33 (USP33) binds [beta]-arrestin2 and leads to the deubiquitination of [beta]-arrestins. USP33 and Mdm2 function reciprocally and favor respectively the stability or lability of the receptor [beta]-arrestin complex, thus regulating the longevity and subcellular localization of receptor signalosomes. Receptors such as the [[beta].sub.2]AR, previously shown to form loose complexes with [beta]-arrestin ("class A") promote a [beta]-arrestin conformation conducive for binding to the deubiquitinase, whereas the vasopressin V2R, which forms tight [beta]-arrestin complexes ("class B"), promotes a distinct [beta]-arrestin conformation that favors dissociation of the enzyme. Thus, USP33-[beta]-arrestin interaction is a key regulatory step in 7TMR trafficking and signal transmission from the activated receptors to downstream effectors. endocytosis | G protein-coupled receptors | ubiquitination | phosphorylation | ERK 1/2
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titleBeta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2.
authorShenoy, Sudha K ; Modi, Aalok S ; Shukla, Arun K ; Xiao, Kunhong ; Berthouze, Magali ; Ahn, Seungkirl ; Wilkinson, Keith D ; Miller, William E ; Lefkowitz, Robert J
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